ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein disulfide-isomerase A4

Intramolecular
Cysteine 91 and cysteine 94 L
Cysteine 206 and cysteine 209 L
Cysteine 84 and cysteine 551 L
A redox-regulated disulphide may form within Protein disulfide-isomerase A4 between cysteines 91 and 94.

Details

Redox score ?
86
PDB code
3idv
Structure name
crystal structure of the a0a fragment of erp72
Structure deposition date
2009-07-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
16
Peptide accession
P13667
Residue number A
91
Residue number B
94
Peptide name
Protein disulfide-isomerase A4

Ligandability

Cysteine 91 of Protein disulfide-isomerase A4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 94 of Protein disulfide-isomerase A4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein disulfide-isomerase A4 between cysteines 206 and 209.

Details

Redox score ?
81
PDB code
3idv
Structure name
crystal structure of the a0a fragment of erp72
Structure deposition date
2009-07-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
18
Peptide accession
P13667
Residue number A
206
Residue number B
209
Peptide name
Protein disulfide-isomerase A4

Ligandability

Cysteine 206 of Protein disulfide-isomerase A4

Not ligandable in the dataset of Yang et al.

Ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 209 of Protein disulfide-isomerase A4

Not ligandable in the dataset of Yang et al.

Ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Protein disulfide-isomerase A4 between cysteines 84 and 551 (37 and 40 respectively in this structure).

Details

Redox score ?
77
PDB code
2dj3
Structure name
the solution structure of the third thioredoxin domain of mouse protein disulfide-isomerase a4
Structure deposition date
2006-03-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
8
Peptide accession
P08003
Residue number A
84
Residue number B
551
Peptide name
Protein disulfide-isomerase A4

Ligandability

Cysteine 84 of Protein disulfide-isomerase A4

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 551 of Protein disulfide-isomerase A4

Not ligandable in the dataset of Yang et al.

Ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

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